Heme biosynthesis in human breast cancer--mimetic "in vitro" studies and some heme enzymic activity levels.
1. Porphyrin biosynthesis from delta-aminolevulinic acid (ALA) was investigated using the technique of tissue explant cultures, in both human breast cancer and its original normal tissue. 2. The activity of ALA-dehydratase, porphobilinogenase and uroporphyrinogen decarboxylase was directly determined in both tumor and normal mammary tissues. 3. Porphyrin synthesis capacity of human breast carcinoma was 20-fold enhanced, as compared with normal tissue, at least between the stages of porphobilinogen and coproporphyrinogen formation. 4. The activity of the three enzymes examined was always lower in normal tissue than in tumoral tissue. 5. Present findings show that porphyrin biosynthesis is increased in breast cancer tissue.
Navone
N M
NM
Centro de Investigaciones sobre Porfirinas y Porfirias (CIPYP) (CONICET-FCEN, UBA), Ciudad Universitaria, Buenos Aires, República Argentina.
Polo
C F
CF
Frisardi
A L
AL
Andrade
N E
NE
Battle
A M
AM
D000328:Adult; D000368:Aged; D000642:Ammonia-Lyases / Q000378:metabolism; D001940:Breast / Q000201:enzymology / Q000378:metabolism; D001943:Breast Neoplasms / Q000201:enzymology / Q000378:metabolism*; D046508:Culture Techniques; D005260:Female; D006418:Heme / Q000096:biosynthesis* / Q000378:metabolism; D006801:Humans; D008875:Middle Aged; D000623:Porphobilinogen Synthase / Q000378:metabolism; D014575:Uroporphyrinogen Decarboxylase / Q000378:metabolism
D006418:Heme; D014575:Uroporphyrinogen Decarboxylase; D000623:Porphobilinogen Synthase; D000642:Ammonia-Lyases; C100132:porphobilinogenase